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Birte Svensson
Birte Svensson
Professor of Enzyme and Protein Chemistry, Technical University of Denmark
Email verificata su bio.dtu.dk
Titolo
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Anno
Relationship of sequence and structure to specificity in the α-amylase family of enzymes
EA MacGregor, Š Janeček, B Svensson
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 2001
8772001
Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability
B Svensson
Plant molecular biology 25, 141-157, 1994
5881994
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
Š Janeček, B Svensson, EA MacGregor
Cellular and molecular life sciences 71, 1149-1170, 2014
3942014
Glucoamylase: structure/function relationships, and protein engineering
J Sauer, BW Sigurskjold, U Christensen, TP Frandsen, E Mirgorodskaya, ...
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 2000
3502000
Crystal and molecular structure of barley α-amylase
A Kadziola, J Abe, B Svensson, R Haser
Journal of molecular biology 239 (1), 104-121, 1994
3281994
Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to …
HM Jespersen, E Ann MacGregor, B Henrissat, MR Sierks, B Svensson
Journal of protein chemistry 12, 791-805, 1993
3211993
Proteome analysis of grain filling and seed maturation in barley
C Finnie, S Melchior, P Roepstorff, B Svensson
Plant Physiology 129 (3), 1308-1319, 2002
3092002
Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs.
E Boel, I Hjort, B Svensson, F Norris, KE Norris, NP Fiil
The EMBO journal 3 (5), 1097-1102, 1984
3011984
Comparison of the domain-level organization of starch hydrolases and related enzymes
HM Jespersen, EA MacGregor, MR Sierks, B Svensson
Biochemical Journal 280 (1), 51-55, 1991
2731991
Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
KH Park, TJ Kim, TK Cheong, JW Kim, BH Oh, B Svensson
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular …, 2000
2652000
Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis
A Kadziola, M Søgaard, B Svensson, R Haser
Journal of Molecular Biology 278 (1), 205-217, 1998
2601998
Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes.
B Svensson, H Jespersen, MR Sierks, EA MacGregor
Biochemical Journal 264 (1), 309, 1989
2591989
The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger
B Svensson, K Larsen, IB Svendsen, E Boel
Carlsberg Research Communications 48, 529-544, 1983
2461983
Proteinaceous α-amylase inhibitors
B Svensson, K Fukuda, PK Nielsen, BC Bønsager
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1696 (2), 145-156, 2004
2412004
Domain evolution in the α-amylase family
S Janecek, B Svensson, B Henrissat
Journal of molecular evolution 45, 322-331, 1997
2351997
The carbohydrate‐binding module family 20–diversity, structure, and function
C Christiansen, M Abou Hachem, Š Janeček, A Viksø‐Nielsen, ...
The FEBS journal 276 (18), 5006-5029, 2009
2322009
A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases
EA MacGregor, HM Jespersen, B Svensson
Febs Letters 378 (3), 263-266, 1996
2121996
Regional distant sequence homology between amylases, α‐glucosidases and transglucanosylases
B Svensson
FEBS letters 230 (1-2), 72-76, 1988
2121988
Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch …
M Søgaard, A Kadziola, R Haser, B Svensson
Journal of Biological Chemistry 268 (30), 22480-22484, 1993
2111993
Characterization of two forms of glucoamylase from Aspergillus niger
B Svensson, TG Svendsen, IB Svendsen, T Sakai, M Ottesen
Carlsberg Research Communications 47, 55-69, 1982
2041982
Il sistema al momento non può eseguire l'operazione. Riprova più tardi.
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